ID Q6BTA5_DEBHA Unreviewed; 557 AA.
AC Q6BTA5;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN OrderedLocusNames=DEHA2D02244g {ECO:0000313|EMBL:CAG86697.2};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG86697.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG86697.2, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; CR382136; CAG86697.2; -; Genomic_DNA.
DR RefSeq; XP_458565.2; XM_458565.1.
DR AlphaFoldDB; Q6BTA5; -.
DR STRING; 284592.Q6BTA5; -.
DR ESTHER; debha-q6bta5; Carboxypeptidase_S10.
DR MEROPS; S10.A49; -.
DR GeneID; 2901448; -.
DR KEGG; dha:DEHA2D02244g; -.
DR VEuPathDB; FungiDB:DEHA2D02244g; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; Q6BTA5; -.
DR OMA; TSCDDTV; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.410; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 19..557
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5005143985"
SQ SEQUENCE 557 AA; 63172 MW; 7391107D38B37F55 CRC64;
MKLSTLIGVL GVVSTTDALS FGMPLMKEIK QSIFKVDVNT ETIDGDAPKE FDFLAEQRKK
LGNIKESFNE DVVYAWEEMQ KKLSPQRLQR KIDEYNSQFK VSSENMNNRV KETFKSYSSG
DDFEVLSADR FADHTLRIKE TNPEVLGLDT VKQYTGYLDV NDLDKHFFYW FFESRNDPEN
DPVILWLNGG PGCSSATGLF FELGPSSINA TLQPEYNPYS WNSNASVIFL DQPVGVGYSY
TNGEEVKSTA SAAKDVFVFL ELFFQKFPQF VKNPFHIAGE SYAGHYIPSF ASEIINHADR
SFDLSSVLIG NGITDSLIQS AYYKPMACGE GGYKQVITDK ECERMEKDYP RCAALTKICY
DAPNALTCVP ANFYCEERLF GPFQKTGLNP YDIRTTCKGD LCYEALGYVD EYLNLDFVKN
VVGASNIEMF NSCDDTVFRN FLFSGDGPKP FQQYVAELLD KNIPVLIYAG DKDFICNWLG
NHGWSDALEY TGHGEFESKP LQPWYTSDKK LAGEVKNHGI FTFLRIYDAG HMVPYDQPEN
ALDMVNRWIQ GDYSYGY
//
